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P48591

- RIR1_DROME

UniProt

P48591 - RIR1_DROME

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Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

RnrL

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.

Catalytic activityi

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

Enzyme regulationi

Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the M1 subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site (By similarity).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei16 – 161Allosteric activatorBy similarity
Binding sitei64 – 641Allosteric activatorBy similarity
Binding sitei99 – 991Allosteric activatorBy similarity
Binding sitei213 – 2131SubstrateBy similarity
Sitei229 – 2291Important for hydrogen atom transferBy similarity
Sitei237 – 2371Allosteric effector binding, determines substrate specificityBy similarity
Binding sitei258 – 2581Substrate; via amide nitrogenBy similarity
Sitei267 – 2671Allosteric effector binding, determines substrate specificityBy similarity
Active sitei438 – 4381Proton acceptorBy similarity
Active sitei440 – 4401Cysteine radical intermediateBy similarity
Active sitei442 – 4421Proton acceptorBy similarity
Sitei455 – 4551Important for hydrogen atom transferBy similarity
Sitei748 – 7481Important for electron transferBy similarity
Sitei749 – 7491Important for electron transferBy similarity
Sitei807 – 8071Interacts with thioredoxin/glutaredoxinBy similarity
Sitei810 – 8101Interacts with thioredoxin/glutaredoxinBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: FlyBase
  2. deoxyribonucleotide biosynthetic process Source: UniProtKB
  3. DNA replication Source: UniProtKB-UniPathway
  4. tissue regeneration Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_212506. Synthesis and interconversion of nucleotide di- and triphosphates.
UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase large subunit (EC:1.17.4.1)
Alternative name(s):
Ribonucleoside-diphosphate reductase subunit M1
Ribonucleotide reductase large subunit
Gene namesi
Name:RnrL
ORF Names:CG5371
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0011703. RnrL.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 812812Ribonucleoside-diphosphate reductase large subunitPRO_0000187193Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi229 ↔ 455Redox-activeBy similarity
Modified residuei778 – 7781Phosphothreonine1 Publication
Modified residuei782 – 7821Phosphoserine1 Publication
Modified residuei786 – 7861Phosphotyrosine1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP48591.

Expressioni

Gene expression databases

BgeeiP48591.

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Protein-protein interaction databases

BioGridi60477. 3 interactions.
DIPiDIP-19582N.
MINTiMINT-829510.

Structurei

3D structure databases

ProteinModelPortaliP48591.
SMRiP48591. Positions 26-753.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 10392ATP-conePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 287Allosteric activator bindingBy similarity
Regioni228 – 2292Substrate bindingBy similarity
Regioni296 – 2994Allosteric effector binding, determines substrate specificityBy similarity
Regioni438 – 4425Substrate bindingBy similarity
Regioni614 – 6185Substrate bindingBy similarity

Sequence similaritiesi

Contains 1 ATP-cone domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0209.
GeneTreeiENSGT00390000001372.
InParanoidiP48591.
KOiK10807.
OMAiEACLMCQ.
OrthoDBiEOG7BGHK2.
PhylomeDBiP48591.

Family and domain databases

InterProiIPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamiPF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF48168. SSF48168. 1 hit.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48591-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLKNKSMKTS KLYVIKRDGR QEEVHFDKIT SRIQKLCYNL NMDFVDPVTI
60 70 80 90 100
TLQVINGLYC GVTTQELDNL AAEIAAGLTC NHPDYAILAA RIAVSNLHKE
110 120 130 140 150
TKKAFSDVFE DLYNHVNKET NQKVPLVSEF HYNVVKKNAT RLNSSIIYDR
160 170 180 190 200
DFGYNYFGFK TLERSYLLKR NGKIAERPQH MLMRVAIGIH GEDIDAAVET
210 220 230 240 250
YNLLSERYFT HASPTLFAAA TNRPQLSSCF LLTMTADSIE GIFKSVEQCA
260 270 280 290 300
MISKSAGGIG LNVHCIRAKG TSICGTNGTS NGLVPMLRVF NNVARYVDQG
310 320 330 340 350
GGKRPGAFAI YLEPWHSDVF EFLELKKNTG KEENRARDLF YALWIPDLFM
360 370 380 390 400
KRVEANGDWS LMCPHKCPGL HDVWGDEFEK LYEKYEQEGR ANRTVKAQSL
410 420 430 440 450
WFAIIEAQVE TGNPYMLFKD ACNRKSNQQN VGTIKCSNLC TEIVEYSAPD
460 470 480 490 500
EIAVCNLASI ALNMFVTPEK TYDFKKLKEV TKIVTKNLNK IIDINYYPLP
510 520 530 540 550
EARKSNLRHR PVGIGIQGFA DALILMRFPY ESEEAGLLNQ QIFETIYYGA
560 570 580 590 600
LEASCELAQT EGPYETYEGS PVSKGILQYD MWDKVPTNLW DWQKLKESIR
610 620 630 640 650
MHGVRNSLLV APMPTASTAQ IMGNNESFEP YTTNIYTRRV LSGEFQVVNH
660 670 680 690 700
HLLRDLTELD LWDDDMKNQI ISSRGSIQNI ETIPPKVRDL YKTVWEISVK
710 720 730 740 750
STIKMAADRG AFIDQSQSFN IHVAEPNYGK LTSIHFYSWK AGLKTGMYYL
760 770 780 790 800
RTKPAANAIQ FTVNKKQGAV SMNGQNGTAE GSPQKYEEDR ERKMADMVCS
810
LENKDACMSC GS
Length:812
Mass (Da):91,978
Last modified:December 1, 2000 - v2
Checksum:i6E4FC608AC04A5FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF52913.2.
AF132143 mRNA. Translation: AAD33590.1.
AY119149 mRNA. Translation: AAM51009.1.
U09369 Genomic DNA. Translation: AAA56995.1.
RefSeqiNP_477027.1. NM_057679.5.
UniGeneiDm.3216.

Genome annotation databases

EnsemblMetazoaiFBtr0080059; FBpp0079648; FBgn0011703.
GeneIDi34392.
KEGGidme:Dmel_CG5371.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF52913.2 .
AF132143 mRNA. Translation: AAD33590.1 .
AY119149 mRNA. Translation: AAM51009.1 .
U09369 Genomic DNA. Translation: AAA56995.1 .
RefSeqi NP_477027.1. NM_057679.5.
UniGenei Dm.3216.

3D structure databases

ProteinModelPortali P48591.
SMRi P48591. Positions 26-753.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 60477. 3 interactions.
DIPi DIP-19582N.
MINTi MINT-829510.

Proteomic databases

PaxDbi P48591.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0080059 ; FBpp0079648 ; FBgn0011703 .
GeneIDi 34392.
KEGGi dme:Dmel_CG5371.

Organism-specific databases

CTDi 34392.
FlyBasei FBgn0011703. RnrL.

Phylogenomic databases

eggNOGi COG0209.
GeneTreei ENSGT00390000001372.
InParanoidi P48591.
KOi K10807.
OMAi EACLMCQ.
OrthoDBi EOG7BGHK2.
PhylomeDBi P48591.

Enzyme and pathway databases

UniPathwayi UPA00326 .
Reactomei REACT_212506. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

GenomeRNAii 34392.
NextBioi 788275.
PROi P48591.

Gene expression databases

Bgeei P48591.

Family and domain databases

InterProi IPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view ]
Pfami PF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view ]
PRINTSi PR01183. RIBORDTASEM1.
SUPFAMi SSF48168. SSF48168. 1 hit.
TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
PROSITEi PS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  4. "Developmental control of a G1-S transcriptional program in Drosophila."
    Duronio R.J., O'Farrell P.H.
    Development 120:1503-1515(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-343.
    Strain: Oregon-R.
  5. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-778; SER-782 AND TYR-786, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiRIR1_DROME
AccessioniPrimary (citable) accession number: P48591
Secondary accession number(s): Q9UB08, Q9VKZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 1, 2000
Last modified: November 26, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3